Alterations in Ca2+ sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers.
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Support for a trimeric collar of myosin binding protein C in cardiac and fast skeletal muscle, but not in slow skeletal musclePhosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?Myosin binding protein C: implications for signal-transductionHypercontractile properties of cardiac muscle fibers in a knock-in mouse model of cardiac myosin-binding protein-CChanges in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin-binding protein C.How do MYBPC3 mutations cause hypertrophic cardiomyopathy?Cardiac myosin binding protein-C gene splice acceptor site mutation is associated with familial hypertrophic cardiomyopathyRadial displacement of myosin cross-bridges in mouse myocardium due to ablation of myosin binding protein-CAblation of myosin-binding protein-C accelerates force development in mouse myocardiumIn the thick of it: HCM-causing mutations in myosin binding proteins of the thick filamentDilated cardiomyopathy in homozygous myosin-binding protein-C mutant miceRegulation of force and unloaded sliding speed in single thin filaments: effects of regulatory proteins and calciumC0 and C1 N-terminal Ig domains of myosin binding protein C exert different effects on thin filament activation.The A31P missense mutation in cardiac myosin binding protein C alters protein structure but does not cause haploinsufficiency.The structure of isolated cardiac Myosin thick filaments from cardiac Myosin binding protein-C knockout mice.Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium.Phosphorylation of cMyBP-C affects contractile mechanisms in a site-specific mannerExpression of masticatory-specific isoforms of myosin heavy-chain, myosin-binding protein-C and tropomyosin in muscle fibers and satellite cell cultures of cat masticatory musclePassive and active tension in single cardiac myofibrilsUnique single molecule binding of cardiac myosin binding protein-C to actin and phosphorylation-dependent inhibition of actomyosin motility requires 17 amino acids of the motif domain.Passive tension in cardiac muscle: contribution of collagen, titin, microtubules, and intermediate filamentsEffects of a non-divalent cation binding mutant of myosin regulatory light chain on tension generation in skinned skeletal muscle fibersThe extent of cardiac myosin binding protein-C phosphorylation modulates actomyosin function in a graded mannerProtein kinase A-induced myofilament desensitization to Ca(2+) as a result of phosphorylation of cardiac myosin-binding protein CTherapeutic potential of c-Myc inhibition in the treatment of hypertrophic cardiomyopathy.Myosin binding protein C: structural abnormalities in familial hypertrophic cardiomyopathy.Altered contractility of skeletal muscle in mice deficient in titin's M-band region.Knockout of p21-activated kinase-1 attenuates exercise-induced cardiac remodelling through altered calcineurin signallingEffect of MyBP-C binding to actin on contractility in heart muscle.Phosphorylation modulates the mechanical stability of the cardiac myosin-binding protein C motif.Knockdown of fast skeletal myosin-binding protein C in zebrafish results in a severe skeletal myopathyCardiac Myosin-binding protein C modulates the tuning of the molecular motor in the heartCardiac myosin-binding protein C: A protein once at loose ends finds its regulatory groove.Slowing of contractile kinetics by myosin-binding protein C can be explained by its cooperative binding to the thin filament.During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation.Designing heart performance by gene transfer.Effects of contractile protein phosphorylation on force development in permeabilized rat cardiac myocytes.Myosin-binding protein C displaces tropomyosin to activate cardiac thin filaments and governs their speed by an independent mechanism.Molecular modulation of actomyosin function by cardiac myosin-binding protein C.Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filaments
P2860
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P2860
Alterations in Ca2+ sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh
1991年學術文章
@zh-hant
name
Alterations in Ca2+ sensitive ...... rabbit skeletal muscle fibers.
@ast
Alterations in Ca2+ sensitive ...... rabbit skeletal muscle fibers.
@en
type
label
Alterations in Ca2+ sensitive ...... rabbit skeletal muscle fibers.
@ast
Alterations in Ca2+ sensitive ...... rabbit skeletal muscle fibers.
@en
prefLabel
Alterations in Ca2+ sensitive ...... rabbit skeletal muscle fibers.
@ast
Alterations in Ca2+ sensitive ...... rabbit skeletal muscle fibers.
@en
P2093
P2860
P356
P1476
Alterations in Ca2+ sensitive ...... rabbit skeletal muscle fibers.
@en
P2093
H C Hartzell
P A Hofmann
P2860
P304
P356
10.1085/JGP.97.6.1141
P577
1991-06-01T00:00:00Z